Structure of peptides and polypeptides in the solid state as elucidated by NMR chemical shift

It is reviewed that through the observation of solid-state C-13 NMR chemical shift, the main-chain conformation and hydrogen-bonded structure of peptides, polypeptides and proteins in the solid state have been successfully elucidated, and the combination of solid stale C-13 NMR and chemical shift calculation by quantum chemistry is a powerful means for the structural characterization. Furthermore, it is briefly introduced that solid state NMR of N-15 and O-17 nuclei is very useful for obtaining information about hydrogen-bonded structure. This review article is communicated on the basis of our recent works on structural characterization of peptides and polypeptides including proteins in the solid state by high-resolution solid-state NMR spectroscopy and its combination with quantum chemical calculation. (C) 1998 Elsevier Science B.V.